Screening for nitric oxide-dependent protein-protein interactions.
Published
Journal Article
Because nitric oxide (NO) may be a ubiquitous regulator of cellular signaling, we have modified the yeast two-hybrid system to explore the possibility of NO-dependent protein-protein interactions. We screened for binding partners of procaspase-3, a protein implicated in apoptotic signaling pathways, and identified multiple NO-dependent interactions.Two such interactions, with acid sphingomyelinase and NO synthase, were shown to occur in mammalian cells dependent on endogenous NO. Nitrosylation may thus provide a broad-based mechanism for regulating interactions between proteins. If so, systematic proteomic analyses in which redox state and NO bioavailability are carefully controlled will reveal a large array of novel interactions.
Full Text
Duke Authors
Cited Authors
- Matsumoto, A; Comatas, KE; Liu, L; Stamler, JS
Published Date
- August 1, 2003
Published In
Volume / Issue
- 301 / 5633
Start / End Page
- 657 - 661
PubMed ID
- 12893946
Pubmed Central ID
- 12893946
Electronic International Standard Serial Number (EISSN)
- 1095-9203
Digital Object Identifier (DOI)
- 10.1126/science.1079319
Language
- eng
Conference Location
- United States